RN128_HUMAN
ID RN128_HUMAN Reviewed; 428 AA.
AC Q8TEB7; A0PJI4; Q6PH80; Q6ZTJ8; Q96RF3; Q9H5E4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=E3 ubiquitin-protein ligase RNF128;
DE EC=2.3.2.27;
DE AltName: Full=Gene related to anergy in lymphocytes protein;
DE Short=GRAIL;
DE AltName: Full=RING finger protein 128;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF128 {ECO:0000305};
DE Flags: Precursor;
GN Name=RNF128;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND MUTAGENESIS.
RX PubMed=12705856; DOI=10.1016/s1074-7613(03)00084-0;
RA Anandasabapathy N., Ford G.S., Bloom D., Holness C., Paragas V.,
RA Seroogy C., Skrenta H., Hollenhorst M., Fathman C.G., Soares L.;
RT "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is
RT expressed in anergic CD4+ T cells.";
RL Immunity 18:535-547(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hepatoma, Lung, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22016387; DOI=10.1074/jbc.m111.222711;
RA Ichikawa D., Mizuno M., Yamamura T., Miyake S.;
RT "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal
RT reorganization through ubiquitination and degradation of Arp2/3 subunit 5
RT and coronin 1A.";
RL J. Biol. Chem. 286:43465-43474(2011).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-204, AND GLYCOSYLATION AT
RP ASN-101.
RG Structural genomics consortium (SGC);
RT "PA domain of the E3 ligase GRAIL.";
RL Submitted (OCT-2009) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains formation. Functions as an
CC inhibitor of cytokine gene transcription. Inhibits IL2 and IL4
CC transcription, thereby playing an important role in the induction of
CC the anergic phenotype, a long-term stable state of T-lymphocyte
CC unresponsiveness to antigenic stimulation associated with the blockade
CC of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages
CC and COR1A with 'Lys-63' linkages leading to their degradation, down-
CC regulation of these cytosleletal components results in impaired
CC lamellipodium formation and reduced accumulation of F-actin at the
CC immunological synapse. Functions in the patterning of the dorsal
CC ectoderm; sensitizes ectoderm to respond to neural-inducing signals.
CC {ECO:0000269|PubMed:12705856, ECO:0000269|PubMed:22016387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q8TEB7; Q92624: APPBP2; NbExp=3; IntAct=EBI-2341619, EBI-743771;
CC Q8TEB7; Q8TAP6: CEP76; NbExp=6; IntAct=EBI-2341619, EBI-742887;
CC Q8TEB7; Q15036: SNX17; NbExp=3; IntAct=EBI-2341619, EBI-1752620;
CC Q8TEB7; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2341619, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12705856, ECO:0000269|PubMed:22016387}. Cytoplasm,
CC perinuclear region {ECO:0000250}. Note=Localized in an asymmetric
CC perinuclear punctate manner. Localizes to the internal pool of the
CC transferrin recycling endosomal pathway. Partially colocalized with the
CC endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and
CC with the late endosomal GTPase RAB7A (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TEB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEB7-2; Sequence=VSP_021685;
CC -!- INDUCTION: Induced under anergic conditions. Up-regulated during T-cell
CC anergy induction following signaling through the T-cell antigen
CC receptor. {ECO:0000269|PubMed:12705856}.
CC -!- DOMAIN: Binding to E2 ubiquitin-conjugating enzyme requires an intact
CC RING finger domain.
CC -!- PTM: Auto-ubiquitinated. Controls the development of T-cell clonal
CC anergy by ubiquitination.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15682.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF394689; AAK77554.1; -; mRNA.
DR EMBL; AK027169; BAB15682.1; ALT_FRAME; mRNA.
DR EMBL; AK074264; BAB85033.1; -; mRNA.
DR EMBL; AK126553; BAC86589.1; -; mRNA.
DR EMBL; AL391315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030951; AAH30951.1; -; mRNA.
DR EMBL; BC056677; AAH56677.1; -; mRNA.
DR EMBL; BC063404; AAH63404.1; -; mRNA.
DR CCDS; CCDS14520.1; -. [Q8TEB7-2]
DR CCDS; CCDS14521.1; -. [Q8TEB7-1]
DR RefSeq; NP_078815.3; NM_024539.3. [Q8TEB7-2]
DR RefSeq; NP_919445.1; NM_194463.1. [Q8TEB7-1]
DR PDB; 3ICU; X-ray; 2.10 A; A=38-204.
DR PDBsum; 3ICU; -.
DR AlphaFoldDB; Q8TEB7; -.
DR SMR; Q8TEB7; -.
DR BioGRID; 122731; 62.
DR IntAct; Q8TEB7; 7.
DR MINT; Q8TEB7; -.
DR STRING; 9606.ENSP00000255499; -.
DR GlyGen; Q8TEB7; 5 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8TEB7; -.
DR PhosphoSitePlus; Q8TEB7; -.
DR BioMuta; RNF128; -.
DR DMDM; 74751443; -.
DR jPOST; Q8TEB7; -.
DR MassIVE; Q8TEB7; -.
DR MaxQB; Q8TEB7; -.
DR PaxDb; Q8TEB7; -.
DR PeptideAtlas; Q8TEB7; -.
DR PRIDE; Q8TEB7; -.
DR ProteomicsDB; 74439; -. [Q8TEB7-1]
DR ProteomicsDB; 74440; -. [Q8TEB7-2]
DR Antibodypedia; 15043; 156 antibodies from 26 providers.
DR DNASU; 79589; -.
DR Ensembl; ENST00000255499.3; ENSP00000255499.2; ENSG00000133135.14. [Q8TEB7-1]
DR Ensembl; ENST00000324342.7; ENSP00000316127.3; ENSG00000133135.14. [Q8TEB7-2]
DR GeneID; 79589; -.
DR KEGG; hsa:79589; -.
DR MANE-Select; ENST00000255499.3; ENSP00000255499.2; NM_194463.2; NP_919445.1.
DR UCSC; uc004emk.4; human. [Q8TEB7-1]
DR CTD; 79589; -.
DR DisGeNET; 79589; -.
DR GeneCards; RNF128; -.
DR HGNC; HGNC:21153; RNF128.
DR HPA; ENSG00000133135; Tissue enhanced (intestine, liver).
DR MIM; 300439; gene.
DR neXtProt; NX_Q8TEB7; -.
DR OpenTargets; ENSG00000133135; -.
DR PharmGKB; PA134868457; -.
DR VEuPathDB; HostDB:ENSG00000133135; -.
DR eggNOG; KOG4628; Eukaryota.
DR GeneTree; ENSGT00940000158347; -.
DR HOGENOM; CLU_049885_0_0_1; -.
DR InParanoid; Q8TEB7; -.
DR OMA; AQSRKQX; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q8TEB7; -.
DR TreeFam; TF317486; -.
DR PathwayCommons; Q8TEB7; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR SignaLink; Q8TEB7; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79589; 14 hits in 734 CRISPR screens.
DR ChiTaRS; RNF128; human.
DR EvolutionaryTrace; Q8TEB7; -.
DR GeneWiki; RNF128; -.
DR GenomeRNAi; 79589; -.
DR Pharos; Q8TEB7; Tbio.
DR PRO; PR:Q8TEB7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8TEB7; protein.
DR Bgee; ENSG00000133135; Expressed in jejunal mucosa and 172 other tissues.
DR ExpressionAtlas; Q8TEB7; baseline and differential.
DR Genevisible; Q8TEB7; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:1904352; P:positive regulation of protein catabolic process in the vacuole; IC:BHF-UCL.
DR GO; GO:0061462; P:protein localization to lysosome; IC:BHF-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..428
FT /note="E3 ubiquitin-protein ligase RNF128"
FT /id="PRO_0000261412"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 75..183
FT /note="PA"
FT ZN_FING 277..318
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 346..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT VAR_SEQ 1..161
FT /note="MGPPPGAGVSCRGGCGFSRLLAWCFLLALSPQAPGSRGAEAVWTAYLNVSWR
FT VPHTGVNRTVWELSEEGVYGQDSPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVWGST
FT VQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHP -> MNQEN
FT RSSFFWLLVIFTFLLKITASFSMSAYVTVTYYNETSNYTAIETCECGVYGLASPVANAM
FT GVVGIPKNNNYQACDHNTEFSNTKKPWIALIERGNCTFSEKIQTAGRRNADAVVIYNAP
FT ETGNQTIQMANF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021685"
FT CONFLICT 4
FT /note="P -> L (in Ref. 1; AAK77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="S -> P (in Ref. 1; AAK77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="V -> G (in Ref. 1; AAK77554)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="I -> L (in Ref. 2; BAB15682)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> G (in Ref. 4; AAH56677)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> L (in Ref. 2; BAB15682)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="V -> A (in Ref. 2; BAB15682)"
FT /evidence="ECO:0000305"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3ICU"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:3ICU"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3ICU"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:3ICU"
SQ SEQUENCE 428 AA; 46521 MW; 32F9CDB32BF208FA CRC64;
MGPPPGAGVS CRGGCGFSRL LAWCFLLALS PQAPGSRGAE AVWTAYLNVS WRVPHTGVNR
TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT NFTVPTVWGS TVQVSWLALI
QRGGGCTFAD KIHLAYERGA SGAVIFNFPG TRNEVIPMSH PGAVDIVAIM IGNLKGTKIL
QSIQRGIQVT MVIEVGKKHG PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ
SRKQRQLKAD AKKAIGRLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH
KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEISNSA SSHEEDNRSE
TASSGYASVQ GTDEPPLEEH VQSTNESLQL VNHEANSVAV DVIPHVDNPT FEEDETPNQE
TAVREIKS
